Publication

Label-Free Detection of Post-translational Modifications with a Nanopore

Restrepo-Pérez, L., Wong, C. H., Maglia, G., Dekker, C. & Joo, C., 13-Nov-2019, In : Nano Letters. 19, 11, p. 7957-7964

Research output: Contribution to journalArticleAcademicpeer-review

Post-translational modifications (PTMs) of proteins play key roles in cellular processes. Hence, PTM identification is crucial for elucidating the mechanism of complex cellular processes and disease. Here we present a method for PTM detection at the single-molecule level using FraC biological nanopores. We focus on two major PTMs, phosphorylation and glycosylation, that mutually compete for protein modification sites, an important regulatory process that has been implicated in the pathogenic pathways of many diseases. We show that phosphorylated and glycosylated peptides can be clearly differentiated from nonmodified peptides by differences in the relative current blockade and dwell time in nanopore translocations. Furthermore, we show that these PTM modifications can be mutually differentiated, demonstrating the identification of phosphorylation and glycosylation in a label-free manner. The results represent an important step for the single-molecule, label-free identification of proteoforms, which have tremendous potential for disease diagnosis and cell biology.

Original languageEnglish
Pages (from-to)7957-7964
JournalNano Letters
Volume19
Issue number11
Early online date18-Oct-2019
Publication statusPublished - 13-Nov-2019

    Keywords

  • PLASMA PROTEOME, PEPTIDES, PHOSPHORYLATION, SPECTROMETRY, TRANSPORT, PORE

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